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151. Two-dimensional electrophoresis

Author

Iwai, Masakazu and Minagawa, Jun

Abstract

3章 単離・精製・活性測定 6. タンパク質 d-1, 光合成反応は多数のタンパク質によって支えられている．それらを網羅的に解析する際，一次元SDS-PAGEでは全てのタンパク質を分離することは困難であるため二次元電気泳動が行われる．本項では，一次元目に等電点電気泳動，二次元目にSDS-PAGEを用いた二次元電気泳動のプロトコルを紹介する．, Two-dimensional electrophoresis (2DE) based on two different principles has been employed to separate many proteins. In this chapter, we describe a protocol for 2DE with isoelectric focusing (IEF) and SDS-PAGE of solubilized thylakoid membranes of C. reinhardtii.

Published
2009

152. Chloroplast-mediated regulation of CO 2 -concentrating mechanism by Ca 2+ -binding protein CAS in the green alga Chlamydomonas reinhardtii

Author

Wang, Lianyong, primary, Yamano, Takashi, additional, Takane, Shunsuke, additional, Niikawa, Yuki, additional, Toyokawa, Chihana, additional, Ozawa, Shin-ichiro, additional, Tokutsu, Ryutaro, additional, Takahashi, Yuichiro, additional, Minagawa, Jun, additional, Kanesaki, Yu, additional, Yoshikawa, Hirofumi, additional, and Fukuzawa, Hideya, additional

Published
2016
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158. The Chlamydomonas Genome Reveals the Evolution of Key Animal and Plant Functions

Author

Mar&#233, Cognat, Val&#233, Fern&#225, Gonz&#225, Lemaire, St&#233, Merchant, Sabeeha S., Prochnik, Simon E., Vallon, Olivier, Harris, Elizabeth H., Karpowicz, Steven J., Witman, George B., Terry, Astrid, Salamov, Asaf, Fritz-Laylin, Lillian K., Marshal, Wallace F., Qu, Liang-Hu, Nelson, David R., Sanderfoot, Anton A., Spalding, Martin H., Kapitonov, Vladimir V., Ren, Qinghu, Ferris, Patrick, Lindquist, Erika, Shapiro, Harris, Lucas, Susan M., Grimwood, Jane, Schmutz, Jeremy, Cardol, Pierre, Cerutti, Heriberto, Chanfreau, Guillaume, Chen, Chun-Long, Croft, Martin T., Dent, Rachel, Dutcher, Susan, Fukuzawa, Hideya, Hallmann, Armin, Hanikenne, Marc, Hippler, Michael, Inwood, William, Jabbari, Kamel, Kalanon, Ming, Kuras, Richard, Lefebvre, Paul A., Loba, Alexey V., Lohr, Martin, Manuell, Andrea, Meier, Iris, Mets, Laurens, Mittag, Maria, Mittelmeier, Telsa, Moroney, James V., Moseley, Jeffrey, Napoli, Carolyn, Nedelcu, Aurora M., Niyogi, Krishna, Novoselov, Sergey V., Paulsen, Ian T., Pazour, Greg, Purton, Saul, Ral, Jean-Philippe, Riano-Pachon, Diego Mauricio, Riekhof, Wayne, Rymarquis, Linda, Schroda, Michael, Stern, David, Umen, James, Willows, Robert, Wilson, Nedra, Zimmer, Sara Lana, Allmer, Jens, Balk, Janneke, Bisova, Katerina, Chen, Chong-Jian, Elias, Marek, Gendler, Karla, Hauser, Charles, Lamb, Mary Rose, Ledford, Heidi, Long, Joanne C., Minagawa, Jun, Page, M. Dudley, Pan, Junmin, Pootakham, Wirulda, Roje, Sanja, Rose, Annkatrin, Stahlberg, Eric, Terauchi, Aimee M., Yang, Pinfen, Ball, Steven, Bowler, Chris, Dieckmann, Carol L., Gladyshev, Vadim N., Green, Pamela, Jorgensen, Richard, Mayfield, Stephen, Mueller-Roeber, Bernd, Rajamani, Sathish, Sayre, Richard T., Brokstein, Peter, Dubchak, Inna, Goodstein, David, Hornick, Leila, Huang, Wayne, Jhaveri, Jinal, Luo, Yigong, Martinez, Diego, Ngau, Wing Chi Abby, Otillar, Bobby, Poliakov, Alexander, Porter, Aaron, Szajkowski, Lukasz, Werner, Gregory, Zhou, Kemin, Grigoriev, Igor V., Rokhsar, Daniel S., and Grossman, Arthur R.

Subjects
food and beverages
Abstract

Chlamydomonas reinhardtii is a unicellular green alga whose lineage diverged from land plants over 1 billion years ago. It is a model system for studying chloroplast-based photosynthesis, as well as the structure, assembly, and function of eukaryotic flagella (cilia), which were inherited from the common ancestor of plants and animals, but lost in land plants. We sequenced the 120-megabase nuclear genome of Chlamydomonas and performed comparative phylogenomic analyses, identifying genes encoding uncharacterized proteins that are likely associated with the function and biogenesis of chloroplasts or eukaryotic flagella. Analyses of the Chlamydomonas genome advance our understanding of the ancestral eukaryotic cell, reveal previously unknown genes associated with photosynthetic and flagellar functions, and establish links between ciliopathy and the composition and function of flagella.

Published
2007

161. Light-Intensity-Dependent Expression of Lhc Gene Family Encoding Light-Harvesting Chlorophyll-a/b Proteins of Photosystem II in Chlamydomonas reinhardtii1

Author

Teramoto, Haruhiko, Nakamori, Akira, Minagawa, Jun, and Ono, Taka-aki

Subjects
Gene Expression Regulation, Light, Diuron, Multigene Family, Algal Proteins, Mutation, Temperature, food and beverages, Animals, Carbon Dioxide, Photosynthesis, Chlamydomonas reinhardtii, Research Article
Abstract

Excessive light conditions repressed the levels of mRNAs accumulation of multiple Lhc genes encoding light-harvesting chlorophyll-a/b (LHC) proteins of photosystem (PS)II in the unicellular green alga, Chlamydomonas reinhardtii. The light intensity required for the repression tended to decrease with lowering temperature or CO(2) concentration. The responses of six LhcII genes encoding the major LHC (LHCII) proteins and two genes (Lhcb4 and Lhcb5) encoding the minor LHC proteins of PSII (CP29 and CP26) were similar. The results indicate that the expression of these Lhc genes is coordinately repressed when the energy input through the antenna systems exceeds the requirement for CO(2) assimilation. The Lhc mRNA level repressed under high-light conditions was partially recovered by adding the electron transport inhibitor 3-(3,4-dichlorophenyl)-1,1-dimethylurea, suggesting that redox signaling via photosynthetic electron carriers is involved in the gene regulation. However, the mRNA level was still considerably lower under high-light than under low-light conditions even in the presence of 3-(3,4-dichlorophenyl)-1,1-dimethylurea. Repression of the Lhc genes by high light was prominent even in the mutants deficient in the reaction center(s) of PSII or both PSI and PSII. The results indicate that two alternative processes are involved in the repression of Lhc genes under high-light conditions, one of which is independent of the photosynthetic reaction centers and electron transport events.

Published
2002

162. Photosystem II Peripheral Accessory Chlorophyll Mutants in Chlamydomonas reinhardtii. Biochemical Characterization and Sensitivity to Photo-Inhibition12

Author

Ruffle, Stuart V., Wang, Jun, Johnston, Heather G., Gustafson, Terry L., Hutchison, Ronald S., Minagawa, Jun, Crofts, Anthony, and Sayre, Richard T.

Subjects
Chlorophyll, Models, Molecular, Manganese, Light, Herbicides, Photosynthetic Reaction Center Complex Proteins, Light-Harvesting Protein Complexes, Photosystem II Protein Complex, Water, Darkness, Ligands, Thylakoids, Electron Transport, Oxygen, Kinetics, Structure-Activity Relationship, Spectrometry, Fluorescence, Diuron, Mutagenesis, Site-Directed, Animals, Photosynthesis, Chlamydomonas reinhardtii, Research Article
Abstract

In addition to the four chlorophylls (Chls) involved in primary charge separation, the photosystem II (PSII) reaction center polypeptides, D1 and D2, coordinate a pair of symmetry-related, peripheral accessory Chls. These Chls are axially coordinated by the D1-H118 and D2-H117 residues and are in close association with the proximal Chl antennae proteins, CP43 and CP47. To gain insight into the function(s) of each of the peripheral Chls, we generated site-specific mutations of the amino acid residues that coordinate these Chls and characterized their energy and electron transfer properties. Our results demonstrate that D1-H118 and D2-H117 mutants differ with respect to: (a) their relative numbers of functional PSII complexes, (b) their relative ability to stabilize charge-separated states, (c) light-harvesting efficiency, and (d) their sensitivity to photo-inhibition. The D2-H117N and D2-H117Q mutants had reduced levels of functional PSII complexes and oxygen evolution capacity as well as reduced light-harvesting efficiencies relative to wild-type cells. In contrast, the D1-H118Q mutant was capable of near wild-type rates of oxygen evolution at saturating light intensities. The D1-H118Q mutant also was substantially more resistant to photo-inhibition than wild type. This reduced sensitivity to photo-inhibition is presumably associated with a reduced light-harvesting efficiency in this mutant. Finally, it is noted that the PSII peripheral accessory Chls have similarities to a to a pair of Chls also present in the PSI reaction center complex.

Published
2001

163. Sucrose density gradient ultracentrifugation

Author

Iwai, Masakazu and Minagawa, Jun

Abstract

3章 単離・精製・活性測定 6. タンパク質 d-2, 光合成反応は，光化学系I，光化学系IIを始め，いくつものタンパク質複合体，あるいはタンパク質超複合体によって行われる．「ショ糖密度勾配超遠心法」は，これらの複合体を大きさによって分画する場合に広く用いられている．本項では，緑藻クラミドモナスの葉緑体上の光化学系複合体を例に取り，ショ糖密度勾配超遠心法のプロトコルを紹介する．, Sucrose density grandient ultracentrifugation has been widely used to separate pigment-binding protein (super) complexes on the photosynthetic membranes. In this chapter, we describe a standard protocol for sucrose density gradient ultracentrifugation of the C. reinhardtii thylakoid membrane proteins.

Published
2009

165. Second-Earth imager for TMT (SEIT): concept and its numerical simulation

Author

Matsuo, Taro, primary, Kotani, Takayuki, additional, Murakami, Naoshi, additional, Kawahara, Hajime, additional, Fujii, Yuka, additional, Oya, Shin, additional, Kurita, Mikio, additional, Natsume, Noriaki, additional, Narita, Norio, additional, Takizawa, Kenji, additional, Ikoma, Masahiro, additional, Minagawa, Jun, additional, Baba, Naoshi, additional, and Tamura, Motohide, additional

Published
2012
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176. The Chlamydomonas Genome Reveals the Evolution of Key Animal and Plant Functions

Author

Merchant, Sabeeha S., primary, Prochnik, Simon E., additional, Vallon, Olivier, additional, Harris, Elizabeth H., additional, Karpowicz, Steven J., additional, Witman, George B., additional, Terry, Astrid, additional, Salamov, Asaf, additional, Fritz-Laylin, Lillian K., additional, Maréchal-Drouard, Laurence, additional, Marshall, Wallace F., additional, Qu, Liang-Hu, additional, Nelson, David R., additional, Sanderfoot, Anton A., additional, Spalding, Martin H., additional, Kapitonov, Vladimir V., additional, Ren, Qinghu, additional, Ferris, Patrick, additional, Lindquist, Erika, additional, Shapiro, Harris, additional, Lucas, Susan M., additional, Grimwood, Jane, additional, Schmutz, Jeremy, additional, Cardol, Pierre, additional, Cerutti, Heriberto, additional, Chanfreau, Guillaume, additional, Chen, Chun-Long, additional, Cognat, Valérie, additional, Croft, Martin T., additional, Dent, Rachel, additional, Dutcher, Susan, additional, Fernández, Emilio, additional, Fukuzawa, Hideya, additional, González-Ballester, David, additional, González-Halphen, Diego, additional, Hallmann, Armin, additional, Hanikenne, Marc, additional, Hippler, Michael, additional, Inwood, William, additional, Jabbari, Kamel, additional, Kalanon, Ming, additional, Kuras, Richard, additional, Lefebvre, Paul A., additional, Lemaire, Stéphane D., additional, Lobanov, Alexey V., additional, Lohr, Martin, additional, Manuell, Andrea, additional, Meier, Iris, additional, Mets, Laurens, additional, Mittag, Maria, additional, Mittelmeier, Telsa, additional, Moroney, James V., additional, Moseley, Jeffrey, additional, Napoli, Carolyn, additional, Nedelcu, Aurora M., additional, Niyogi, Krishna, additional, Novoselov, Sergey V., additional, Paulsen, Ian T., additional, Pazour, Greg, additional, Purton, Saul, additional, Ral, Jean-Philippe, additional, Riaño-Pachón, Diego Mauricio, additional, Riekhof, Wayne, additional, Rymarquis, Linda, additional, Schroda, Michael, additional, Stern, David, additional, Umen, James, additional, Willows, Robert, additional, Wilson, Nedra, additional, Zimmer, Sara Lana, additional, Allmer, Jens, additional, Balk, Janneke, additional, Bisova, Katerina, additional, Chen, Chong-Jian, additional, Elias, Marek, additional, Gendler, Karla, additional, Hauser, Charles, additional, Lamb, Mary Rose, additional, Ledford, Heidi, additional, Long, Joanne C., additional, Minagawa, Jun, additional, Page, M. Dudley, additional, Pan, Junmin, additional, Pootakham, Wirulda, additional, Roje, Sanja, additional, Rose, Annkatrin, additional, Stahlberg, Eric, additional, Terauchi, Aimee M., additional, Yang, Pinfen, additional, Ball, Steven, additional, Bowler, Chris, additional, Dieckmann, Carol L., additional, Gladyshev, Vadim N., additional, Green, Pamela, additional, Jorgensen, Richard, additional, Mayfield, Stephen, additional, Mueller-Roeber, Bernd, additional, Rajamani, Sathish, additional, Sayre, Richard T., additional, Brokstein, Peter, additional, Dubchak, Inna, additional, Goodstein, David, additional, Hornick, Leila, additional, Huang, Y. Wayne, additional, Jhaveri, Jinal, additional, Luo, Yigong, additional, Martínez, Diego, additional, Ngau, Wing Chi Abby, additional, Otillar, Bobby, additional, Poliakov, Alexander, additional, Porter, Aaron, additional, Szajkowski, Lukasz, additional, Werner, Gregory, additional, Zhou, Kemin, additional, Grigoriev, Igor V., additional, Rokhsar, Daniel S., additional, and Grossman, Arthur R., additional

Published
2007
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177. PHOTOSYSTEM II SUBUNIT R Is Required for Efficient Binding of LIGHT-HARVESTING COMPLEX STRESS-RELATED PROTEIN3 to Photosystem II-Light-Harvesting Supercomplexes in Chlamydomonas reinhardtii.

Author

Huidan Xue, Ryutaro Tokutsu, Bergner, Sonja Verena, Scholz, Martin, Minagawa, Jun, and Hippler, Michael

Subjects
CHLAMYDOMONAS reinhardtii, PHOTOSYSTEMS, PROTEIN binding, PROTEOMICS, MEMBRANE proteins
Abstract

In Chlamydomonas reinhardtii, the LIGHT-HARVESTING COMPLEX STRESS-RELATED PROTEIN3 (LHCSR3) protein is crucial for efficient energy-dependent thermal dissipation of excess absorbed light energy and functionally associates with photosystem II-light-harvesting complex II (PSII-LHCII) supercomplexes. Currently, it is unknown how LHCSR3 binds to the PSII-LHCII supercomplex. In this study, we investigated the role of PHOTOSYSTEM II SUBUNIT R (PSBR) an intrinsic membrane-spanning PSII subunit, in the binding of LHCSR3 to PSII-LHCII supercomplexes. Down-regulation of PSBR expression diminished the efficiency of oxygen evolution and the extent of nonphotochemical quenching and had an impact on the stability of the oxygen-evolving complex as well as on PSII-LHCII-LHCSR3 supercomplex formation. Its down-regulation destabilized the PSII-LHCII supercomplex and strongly reduced the binding of LHCSR3 to PSII-LHCII supercomplexes, as revealed by quantitative proteomics. PHOTOSYSTEM II SUBUNIT P deletion, on the contrary, destabilized PHOTOSYSTEM II SUBUNIT Q binding but did not affect PSBR and LHCSR3 association with PSII-LHCII. In summary, these data provide clear evidence that PSBR is required for the stable binding of LHCSR3 to PSII-LHCII supercomplexes and is essential for efficient energy-dependent quenching and the integrity of the PSII-LHCIILHCSR3 supercomplex under continuous high light. [ABSTRACT FROM AUTHOR]

Published
2015
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180. Establishment of publicly available cDNA material and information resource of Chlamydomonas reinhardtii (Chlorophyta) to facilitate gene function analysis

Author

Asamizu, Erika, primary, Nakamura, Yasukazu, additional, Miura, Kenji, additional, Fukuzawa, Hideya, additional, Fujiwara, Shoko, additional, Hirono, Masafumi, additional, Iwamoto, Koji, additional, Matsuda, Yoshihiro, additional, Minagawa, Jun, additional, Shimogawara, Kosuke, additional, Takahashi, Yuichiro, additional, and Tabata, Satoshi, additional

Published
2004
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187. A blue-light photoreceptor mediates the feedback regulation of photosynthesis

Author

Petroutsos, Dimitris, Tokutsu, Ryutaro, Maruyama, Shinichiro, Flori, Serena, Greiner, Andre, Magneschi, Leonardo, Cusant, Loic, Kottke, Tilman, Mittag, Maria, Hegemann, Peter, Finazzi, Giovanni, and Minagawa, Jun

Abstract

Algae rely on blue-light-sensitive phototropin to trigger induction of LHCRS3, allowing it to dissipate energy from excess light that would otherwise compromise the fitness of the organism.

Published
2016
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188. Chloroplast remodeling during state transitions in Chlamydomonas reinhardtii as revealed by noninvasive techniques in vivo.

Author

Nagy, Gergely, Ünnep, Renáta, Ottó Zsiros, Ryutaro Tokutsu, Kenji Takizawa, Porcar, Lionel, Moyet, Lucas, Petroutsos, Dimitris, Győző Garab, Finazzi, Giovanni, and Minagawa, Jun

Subjects
PHOTOSYNTHESIS, PLANTS, EXTRACHROMOSOMAL DNA, OPTICAL polarization, ALGORITHMS
Abstract

Plants respond to changes in light quality by regulating the absorption capacity of their photosystems. These short-term adaptations use redox-controlled, reversible phosphorylation of the lightharvesting complexes (LHCIIs) to regulate the relative absorption cross-section of the two photosystems (PSs), commonly referred to as state transitions. It is acknowledged that state transitions induce substantial reorganizations of the PSs. However, their consequences on the chloroplast structure are more controversial. Here, we investigate how state transitions affect the chloroplast structure and function using complementary approaches for the living cells of Chlamydomonas reinhardtii. Using small-angle neutron scattering, we found a strong periodicity of the thylakoids in state 1, with characteristic repeat distances of ~200 Å, which was almost completely lost in state 2. As revealed by circular dichroism, changes in the thylakoid periodicity were paralleled by modifications in the long-range order arrangement of the photosynthetic complexes, which was reduced by ~20% in state 2 compared with state 1, but was not abolished. Furthermore, absorption spectroscopy reveals that the enhancement of PSI antenna size during state 1 to state 2 transition (~20%) is not commensurate to the decrease in PSII antenna size (~70%), leading to the possibility that a large part of the phosphorylated LHCIIs do not bind to PSI, but instead form energetically quenched complexes, which were shown to be either associated with PSII supercomplexes or in a free form. Altogether these noninvasive in vivo approaches allow us to present a more likely scenario for state transitions that explains their molecular mechanism and physiological consequences. [ABSTRACT FROM AUTHOR]

Published
2014
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197. Energy-dissipative supercomplex of photosystem II associated with LHCSR3 in Chlamydomonas reinhardtii.

Author

Tokutsu, Ryutaro and Minagawa, Jun

Subjects
*PHOTOSYSTEM II inhibitors, *GREEN algae, *HYDROGEN-ion concentration, *LUMINESCENCE, *AQUATIC resources, *ORGANIC acids
Abstract

Plants and green algae have a low pH-inducible mechanism in photosystem II (PSII) that dissipates excess light energy, measured as the nonphotochemical quenching of chlorophyll fluorescence (qE). Recently, nonphotochemical quenching 4 (npq4), a mutant strain of the green alga Chlamydomonas reinhardtii that is qE-deficient and lacks the light-harvesting complex stress-related protein 3 (LHCSR3), was reported [Peers G, et al. (2009) Nature 462(7272):518-521]. Here, applying a newly established procedure, we isolated the PSII supercomplex and its associated light-harvesting proteins from both WT C. reinhardtii and the npq4 mutant grown in either low light (LL) or high light (HL). LHCSR3 was present in the PSII supercomplex from the HL-grown WT, but not in the supercomplex from the LL-grown WT or mutant. The purified PSII supercomplex containing LHCSR3 exhibited a normal fluorescence lifetime at a neutral pH (7.5) by single-photon counting analysis, but a significantly shorter lifetime at pH 5.5, which mimics the acidified lumen of the thylakoid membranes in HL-exposed chloroplasts. The switch from light-harvesting mode to energy-dissipating mode observed in the LHCSR3-containing PSII supercomplex was sensitive to dicyclohexylcarbodiimide, a protein-modifying agent specific to protonatable amino acid residues. We conclude that the PSII-LHCII-LHCSR3 supercomplex formed in the HL-grown C. reinhardtii cells is capable of energy dissipation on protonation of LHCSR3. [ABSTRACT FROM AUTHOR]

Published
2013
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198. Dual Strategy to Cope with High Light in Chlamydomonas reinhardtii.

Author

Allorent, Guillaume, Tokutsu, Ryutaro, Roach, Thomas, Peers, Graham, Cardol, Pierre, Girard-Bascou, Jacqueline, Seigneurin-Berny, Daphné, Petroutsos, Dimitris, Kuntz, Marcel, Breyton, Cécile, Franck, Fabrice, Wollman, Francis-André, Niyogi, Krishna K., Krieger-Liszkay, Anja, Minagawa, Jun, and Finazzi, Giovanni

Subjects
CHLAMYDOMONAS reinhardtii, CHLAMYDOMONAS, LIGHT absorption, ANTENNAS (Electronics), ELECTRON transport, ENERGY dissipation
Abstract

Absorption of light in excess of the capacity for photosynthetic electron transport is damaging to photosynthetic organisms. Several mechanisms exist to avoid photodamage, which are collectively referred to as nonphotochemical quenching. This term comprises at least two major processes. State transitions (qT) represent changes in the relative antenna sizes of photosystems II and I. High energy quenching (qE) is the increased thermal dissipation of light energy triggered by lumen acidification. To investigate the respective roles of qE and qT in photoprotection, a mutant (npq4 stt7-9) was generated in Chlamydomonas reinhardtii by crossing the state transition–deficient mutant (stt7-9) with a strain having a largely reduced qE capacity (npq4). The comparative phenotypic analysis of the wild type, single mutants, and double mutants reveals that both state transitions and qE are induced by high light. Moreover, the double mutant exhibits an increased photosensitivity with respect to the single mutants and the wild type. Therefore, we suggest that besides qE , state transitions also play a photoprotective role during high light acclimation of the cells, most likely by decreasing hydrogen peroxide production. These results are discussed in terms of the relative photoprotective benefit related to thermal dissipation of excess light and/or to the physical displacement of antennas from photosystem II. [ABSTRACT FROM AUTHOR]

Published
2013
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199. Live-cell imaging of photosystem II antenna dissociation during state transitions.

Author

Iwai, Masakazu, Yokono, Makio, Inada, Noriko, and Minagawa, Jun

Subjects
PHOTOSYNTHESIS, EFFECT of light on plants, ENERGY dissipation, GREEN algae, FLUORESCENCE spectroscopy
Abstract

Plants and green algae maintain efficient photosynthesis under changing light environments by adjusting their light-harvesting capacity. It has been suggested that energy redistribution is brought about by shuttling the light-harvesting antenna complex II (LHCII) between photosystem II (PSII) and photosystem I (PSI) (state transitions), but such molecular remodeling has never been demonstrated in vivo. Here, using chlorophyll fluorescence lifetime imaging microscopy, we visualized phospho-LHCII dissociation from PSII in live cells of the green alga Chiamydomonas reinhardtii. Induction of energy redistribution in wild-type cells led to an increase in, and spreading of, a 250-ps lifetime chlorophyll fluorescence component, which was not observed in the stt7 mutant incapable of state transitions. The 250-ps component was also the dominant component ma mutant containing the light-harvesting antenna complexes but no photosystems. The appearance of the 250-ps component was accompanied by activation of LHCII phosphorylation, supporting the visualization of phospho-LHCII dissociation. Possible implications of the unbound phospho-LHCII on energy dissipation are discussed. [ABSTRACT FROM AUTHOR]

Published
2010
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